Interaction of Structurally Diverse Phenolic Compounds with Porcine Pancreatic α-Amylase

被引：43

作者：

Kaeswurm, Julia A. H. ^{[1
]}

Claasen, Birgit ^{[2
]}

Fischer, Max -Philipp ^{[3
]}

Buchweitz, Maria ^{[1
]}

机构：

[1] Univ Stuttgart, Inst Biochem & Tech Biochem, Dept Food Chem, Allmandring 5b, D-70569 Stuttgart, Germany

[2] Univ Stuttgart, Inst Organ Chem, Pfaffenwaldring 55, D-70569 Stuttgart, Germany

[3] Univ Stuttgart, Inst Biochem & Tech Biochem, Dept Tech Biochem, Allmandring 31, D-70569 Stuttgart, Germany

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2019年 / 67卷 / 40期

关键词：

alpha-amylase; polyphenols; inhibition kinetics; binding epitope; saturation transfer difference (STD)-NMR; isothermal titration calorimetry (ITC); TRANSFER DIFFERENCE NMR; DIETARY POLYPHENOLS; TEA POLYPHENOLS; LIGAND-BINDING; IN-VITRO; INHIBITION; GLUCOSIDASE; KINETICS; ANTHOCYANINS; CALORIMETRY;

D O I：

10.1021/acs.jafc.9b04798

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

A blood glucose level lowering effect is postulated for polyphenols (PPs), which is in part attributed to the inhibition of alpha-amylase. To estimate structure-effect relationships, chlorogenic acid (CA), phlorizin (PHL), epigallocatechin gallate (EGCG), epicatechin (EC), and malvidin-3-glucoside (Mlv-3-glc) were used as inhibitors in an enzyme assay, on the basis of the conversion of GalG(2)CNP by alpha-amylase. The detection of CNP was performed by UV/vis spectroscopy. The data reveal that the inhibitor strength decreases as follows: EGCG > Mlv-3-glc > EC > PHL similar to CA. Detection of the substrate conversion by isothermal titration calorimetry supports these results. All PPs showed mixed inhibition, except for CA and EGCG wherein the competitive proportion was predominant. Investigations by saturation transfer difference NMR revealed interaction of PPs with alpha-amylase prevalently based on interactions with the aromatic or conjugated system. A correlation between the extent of the conjugated system and the IC50 of the PP could be found.

引用

页码：11108 / 11118

页数：11

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